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4JGY

Crystal structure of human coxsackievirus A16 uncoating intermediate (space group P4232)

Summary for 4JGY
Entry DOI10.2210/pdb4jgy/pdb
DescriptorPolyprotein, capsid protein VP1, Polyprotein, capsid protein VP2, Polyprotein, capsid protein VP3 (3 entities in total)
Functional Keywordsvirus, hand-foot-and-mouth disease, picornavirus uncoating, pocket factor, icosahedral virus
Biological sourceHuman coxsackievirus A16
More
Cellular locationPicornain 3C: Host cytoplasm (By similarity). Protein 3B: Virion (By similarity): I3W9E1 I3W9E1 I3W9E1
Total number of polymer chains3
Total formula weight87331.78
Authors
Primary citationRen, J.,Wang, X.,Hu, Z.,Gao, Q.,Sun, Y.,Li, X.,Porta, C.,Walter, T.S.,Gilbert, R.J.,Zhao, Y.,Axford, D.,Williams, M.,McAuley, K.,Rowlands, D.J.,Yin, W.,Wang, J.,Stuart, D.I.,Rao, Z.,Fry, E.E.
Picornavirus uncoating intermediate captured in atomic detail.
Nat Commun, 4:1929-1929, 2013
Cited by
PubMed Abstract: It remains largely mysterious how the genomes of non-enveloped eukaryotic viruses are transferred across a membrane into the host cell. Picornaviruses are simple models for such viruses, and initiate this uncoating process through particle expansion, which reveals channels through which internal capsid proteins and the viral genome presumably exit the particle, although this has not been clearly seen until now. Here we present the atomic structure of an uncoating intermediate for the major human picornavirus pathogen CAV16, which reveals VP1 partly extruded from the capsid, poised to embed in the host membrane. Together with previous low-resolution results, we are able to propose a detailed hypothesis for the ordered egress of the internal proteins, using two distinct sets of channels through the capsid, and suggest a structural link to the condensed RNA within the particle, which may be involved in triggering RNA release.
PubMed: 23728514
DOI: 10.1038/ncomms2889
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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